6EHS
E. coli Hydrogenase-2 chemically reduced structure
Summary for 6EHS
| Entry DOI | 10.2210/pdb6ehs/pdb |
| Related | 6EHQ |
| Descriptor | Hydrogenase-2 small chain, Hydrogenase-2 large chain, IRON/SULFUR CLUSTER, ... (9 entities in total) |
| Functional Keywords | hydrogen oxidation, membrane protein, nife hydrogenase, oxidoreductase |
| Biological source | Escherichia coli More |
| Cellular location | Cell membrane; Peripheral membrane protein; Periplasmic side: P69741 Cell membrane; Peripheral membrane protein: P0ACE0 |
| Total number of polymer chains | 4 |
| Total formula weight | 190308.38 |
| Authors | Carr, S.B.,Evans, R.M.,Beaton, S.E.,Armstrong, F.A. (deposition date: 2017-09-15, release date: 2018-04-18, Last modification date: 2024-11-06) |
| Primary citation | Beaton, S.E.,Evans, R.M.,Finney, A.J.,Lamont, C.M.,Armstrong, F.A.,Sargent, F.,Carr, S.B. The structure of hydrogenase-2 fromEscherichia coli: implications for H2-driven proton pumping. Biochem. J., 475:1353-1370, 2018 Cited by PubMed Abstract: Under anaerobic conditions, is able to metabolize molecular hydrogen via the action of several [NiFe]-hydrogenase enzymes. Hydrogenase-2, which is typically present in cells at low levels during anaerobic respiration, is a periplasmic-facing membrane-bound complex that functions as a proton pump to convert energy from hydrogen (H) oxidation into a proton gradient; consequently, its structure is of great interest. Empirically, the complex consists of a tightly bound core catalytic module, comprising large (HybC) and small (HybO) subunits, which is attached to an Fe-S protein (HybA) and an integral membrane protein (HybB). To date, efforts to gain a more detailed picture have been thwarted by low native expression levels of Hydrogenase-2 and the labile interaction between HybOC and HybA/HybB subunits. In the present paper, we describe a new overexpression system that has facilitated the determination of high-resolution crystal structures of HybOC and, hence, a prediction of the quaternary structure of the HybOCAB complex. PubMed: 29555844DOI: 10.1042/BCJ20180053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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